, Orthomyxoviruses, 2007.
An overlapping protein-coding region in influenza A virus segment 3 modulates the host response, Science, vol.337, pp.199-204, 2012. ,
Identification of novel influenza A virus proteins translated from PA mRNA, J. Virol, vol.87, pp.2455-2462, 2013. ,
Molecular mechanisms enhancing the proteome of influenza A viruses: an overview of recently discovered proteins, Virus Res, vol.185, pp.53-63, 2014. ,
A complicated message: identification of a novel PB1-related protein translated from influenza A virus segment 2 mRNA, J. Virol, vol.83, pp.8021-8031, 2009. ,
Identification of a novel splice variant form of the influenza A virus M2 ion channel with an antigenically distinct ectodomain, PLoS Pathog, vol.8, p.1002998, 2012. ,
A novel influenza A virus mitochondrial protein that induces cell death, Nat. Med, vol.7, pp.1306-1312, 2001. ,
Current knowledge on PB1-F2 of influenza A viruses, Med. Microbiol. Immunol, vol.200, pp.69-75, 2011. ,
Genomic analysis of increased host immune and cell death responses induced by 1918 influenza virus, Nature, vol.443, pp.578-581, 2006. ,
A question of self-preservation: immunopathology in influenza virus infection, Immunol. Cell Biol, vol.85, pp.85-92, 2007. ,
Expression of the 1918 influenza A virus PB1-F2 enhances the pathogenesis of viral and secondary bacterial pneumonia, Cell Host Microbe, vol.2, pp.240-249, 2007. ,
An insight into the PB1F2 protein and its multifunctional role in enhancing the pathogenicity of the influenza A viruses, Virology, vol.440, pp.97-104, 2013. ,
The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function, J. Virol, vol.77, pp.7214-7224, 2003. ,
Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria, FEBS Lett, vol.578, pp.331-336, 2004. ,
Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity, Nat. Commun, vol.5, p.4713, 2014. ,
Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1, PLoS Pathog, vol.1, p.4, 2005. ,
PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes, J. Virol, vol.78, pp.6304-6312, 2004. ,
The proapoptotic influenza A virus protein PB1-F2 forms a nonselective ion channel, PLoS ONE, vol.5, p.11112, 2010. ,
The proapoptotic influenza A virus protein PB1-F2 regulates viral polymerase activity by interaction with the PB1 protein, Cell Microbiol, vol.10, pp.1140-1152, 2008. ,
The effects of influenza A virus PB1-F2 protein on polymerase activity are strain specific and do not impact pathogenesis, J. Virol, vol.84, pp.558-564, 2010. ,
A single N66S mutation in the PB1-F2 protein of influenza A virus increases virulence by inhibiting the early interferon response in vivo, J. Virol, vol.85, pp.652-662, 2011. ,
Influenza A virus protein PB1-F2 exacerbates IFN-? expression of human respiratory epithelial cells, J. Immunol, vol.185, pp.4812-4823, 2010. ,
URL : https://hal.archives-ouvertes.fr/hal-01193647
Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential, J. Virol, vol.86, pp.8359-8366, 2012. ,
The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein, PLoS Pathog, vol.7, p.1002067, 2011. ,
A novel cytotoxic sequence contributes to influenza A viral protein PB1-F2 pathogenicity and predisposition to secondary bacterial infection, J. Virol, vol.88, pp.503-515, 2014. ,
Naturally occurring swine influenza A virus PB1-F2 phenotypes that contribute to superinfection with Gram-positive respiratory pathogens, J. Virol, vol.86, pp.9035-9043, 2012. ,
-F2 influenza A virus protein adopts a ?-sheet conformation and forms amyloid fibers in membrane environments, J. Biol. Chem, vol.285, pp.13233-13243, 2010. ,
Direct electrochemical detection of PB1-F2 protein of influenza A virus in infected cells, Biosens. Bioelectron, vol.59, pp.6-13, 2014. ,
URL : https://hal.archives-ouvertes.fr/hal-02635315
Detection of soluble oligomers formed by PB1-F2 influenza A virus protein in vitro, J. Anal. Bioanal. Tech, vol.4, p.169, 2013. ,
URL : https://hal.archives-ouvertes.fr/hal-02642907
Molecular mechanism of thioflavin-T binding to amyloid fibrils, Biochim. Biophys. Acta, vol.1804, pp.1405-1412, 2010. ,
Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by ?-helical antimicrobial and cell nonselective membrane-lytic peptides, Biochim. Biophys. Acta, vol.1462, pp.55-70, 1999. ,
Mechanisms of antimicrobial peptide action and resistance, Pharmacol. Rev, vol.55, pp.27-55, 2003. ,
Tetrazolium dyes as tools in cell biology: new insights into their cellular reduction, Biotechnol. Annu. Rev, vol.11, pp.127-152, 2005. ,
Electrochemical detection of the oligomerization of PB1-F2 influenza A virus protein in infected cells, Anal. Chem, vol.86, pp.9098-9105, 2014. ,
URL : https://hal.archives-ouvertes.fr/hal-02635306
Transcriptomic analysis of host immune and cell death responses associated with the influenza A virus PB1-F2 protein, PLoS Pathog, vol.7, p.1002202, 2011. ,
URL : https://hal.archives-ouvertes.fr/hal-00684735
Flow cytometry of apoptotic cell death, J. Immunol. Methods, vol.243, pp.167-190, 2000. ,
Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice, J. Virol, vol.80, pp.7976-7983, 2006. ,
The multifaceted effect of PB1-F2 specific antibodies on influenza A virus infection, Virology, vol.447, pp.1-8, 2013. ,
?2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH, PLoS ONE, vol.9, p.104492, 2014. ,
Biosensing of lipid-prion interactions: insights on charge effect, Cu(II)-ions binding and prion oligomerization, Biosens. Bioelectron, vol.26, pp.1399-1406, 2010. ,
Lysozyme: a model protein for amyloid research, Adv. Protein. Chem. Struct. Biol, vol.84, pp.63-111, 2011. ,
Direct observation of the interconversion of normal and toxic forms of ?-synuclein, Cell, vol.149, pp.1048-1059, 2012. ,
Wild-type Shadoo proteins convert to amyloid-like forms under native conditions, J. Neurochem, vol.113, pp.92-104, 2010. ,
Shadoo binds lipid membranes and undergoes aggregation and fibrillization, Biochem. Biophys. Res. Commun, vol.438, pp.519-525, 2013. ,
URL : https://hal.archives-ouvertes.fr/hal-02643069
Small liposomes accelerate the fibrillation of amyloid ?(1-40), J. Biol. Chem, vol.290, pp.815-826, 2015. ,
Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers, J. Mol. Biol, vol.376, pp.42-54, 2008. ,
Probing the interplay between amyloidogenic proteins and membranes using lipid monolayers and bilayers, Adv. Colloid Interface Sci, vol.207, pp.81-92, 2014. ,
Mechanism of membrane interaction and disruption by ?-synuclein, J. Am. Chem. Soc, vol.133, pp.19366-19375, 2011. ,
The mechanism of membrane disruption by cytotoxic amyloid oligomers formed by prion protein(106 -126) is dependent on bilayer composition, J. Biol. Chem, vol.289, pp.10419-10430, 2014. ,
Prefibrillar amyloid protein aggregates share common features of cytotoxicity, J. Biol. Chem, vol.279, pp.31374-31382, 2004. ,
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases, Nature, vol.416, pp.507-511, 2002. ,
Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases, J. Biol. Chem, vol.279, pp.46363-46366, 2004. ,
Activation of the NLRP3 inflammasome by IAV virulence protein PB1-F2 contributes to severe pathophysiology and disease, PLoS Pathog, vol.9, p.1003392, 2013. ,
,
,
, Amyloid Assemblies of Influenza A Virus PB1-F2 Protein Damage Membrane, vol.291, pp.739-751, 2015.
, J. Biol. Chem
, Access the most updated version of this article at doi: Alerts: When a correction for this article is posted ? When this article is cited ?